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Volumn 7, Issue 12, 2011, Pages

Inhibition of apoptosis and NF-κB activation by vaccinia protein N1 occur via distinct binding surfaces and make different contributions to virulence

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN BCL 2; UNCLASSIFIED DRUG; VACCINIA VIRUS PROTEIN N1; VIRUS PROTEIN;

EID: 84855265610     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002430     Document Type: Article
Times cited : (74)

References (63)
  • 1
    • 70349918182 scopus 로고    scopus 로고
    • NFkB inhibitors: strategies from poxviruses
    • Mohamed MR, McFadden G, (2009) NFkB inhibitors: strategies from poxviruses. Cell Cycle 8: 3125-3132.
    • (2009) Cell Cycle , vol.8 , pp. 3125-3132
    • Mohamed, M.R.1    McFadden, G.2
  • 3
    • 0036328156 scopus 로고    scopus 로고
    • The vaccinia virus N1L protein is an intracellular homodimer that promotes virulence
    • Bartlett N, Symons JA, Tscharke DC, Smith GL, (2002) The vaccinia virus N1L protein is an intracellular homodimer that promotes virulence. J Gen Virol 83: 1965-1976.
    • (2002) J Gen Virol , vol.83 , pp. 1965-1976
    • Bartlett, N.1    Symons, J.A.2    Tscharke, D.C.3    Smith, G.L.4
  • 4
    • 56349162153 scopus 로고    scopus 로고
    • Vaccinia virus lacking the Bcl-2-like protein N1 induces a stronger natural killer cell response to infection
    • Jacobs N, Bartlett NW, Clark RH, Smith GL, (2008) Vaccinia virus lacking the Bcl-2-like protein N1 induces a stronger natural killer cell response to infection. J Gen Virol 89: 2877-2881.
    • (2008) J Gen Virol , vol.89 , pp. 2877-2881
    • Jacobs, N.1    Bartlett, N.W.2    Clark, R.H.3    Smith, G.L.4
  • 5
    • 0024345810 scopus 로고
    • Mapping and insertional mutagenesis of a vaccinia virus gene encoding a 13,800-Da secreted protein
    • Kotwal GJ, Hugin AW, Moss B, (1989) Mapping and insertional mutagenesis of a vaccinia virus gene encoding a 13,800-Da secreted protein. Virology 171: 579-587.
    • (1989) Virology , vol.171 , pp. 579-587
    • Kotwal, G.J.1    Hugin, A.W.2    Moss, B.3
  • 6
    • 33845920705 scopus 로고    scopus 로고
    • Vaccinia virus N1L protein resembles a B cell lymphoma-2 (Bcl-2) family protein
    • Aoyagi M, Zhai D, Jin C, Aleshin AE, Stec B, et al. (2007) Vaccinia virus N1L protein resembles a B cell lymphoma-2 (Bcl-2) family protein. Protein Sci 16: 118-124.
    • (2007) Protein Sci , vol.16 , pp. 118-124
    • Aoyagi, M.1    Zhai, D.2    Jin, C.3    Aleshin, A.E.4    Stec, B.5
  • 7
    • 50849109845 scopus 로고    scopus 로고
    • Vaccinia virus proteins A52 and B14 Share a Bcl-2-like fold but have evolved to inhibit NF-kappaB rather than apoptosis
    • Graham SC, Bahar MW, Cooray S, Chen RA, Whalen DM, et al. (2008) Vaccinia virus proteins A52 and B14 Share a Bcl-2-like fold but have evolved to inhibit NF-kappaB rather than apoptosis. PLoS Pathog 4: e1000128.
    • (2008) PLoS Pathog , vol.4
    • Graham, S.C.1    Bahar, M.W.2    Cooray, S.3    Chen, R.A.4    Whalen, D.M.5
  • 8
    • 34249787896 scopus 로고    scopus 로고
    • Functional and structural studies of the vaccinia virus virulence factor N1 reveal a Bcl-2-like anti-apoptotic protein
    • Cooray S, Bahar MW, Abrescia NG, McVey CE, Bartlett NW, et al. (2007) Functional and structural studies of the vaccinia virus virulence factor N1 reveal a Bcl-2-like anti-apoptotic protein. J Gen Virol 88: 1656-1666.
    • (2007) J Gen Virol , vol.88 , pp. 1656-1666
    • Cooray, S.1    Bahar, M.W.2    Abrescia, N.G.3    McVey, C.E.4    Bartlett, N.W.5
  • 10
    • 58149107158 scopus 로고    scopus 로고
    • Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3
    • Kalverda AP, Thompson GS, Vogel A, Schroder M, Bowie AG, et al. (2009) Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3. J Mol Biol 385: 843-853.
    • (2009) J Mol Biol , vol.385 , pp. 843-853
    • Kalverda, A.P.1    Thompson, G.S.2    Vogel, A.3    Schroder, M.4    Bowie, A.G.5
  • 11
    • 79957987060 scopus 로고    scopus 로고
    • Mapping the IkappaB kinase beta (IKKbeta)-binding interface of the B14 protein, a vaccinia virus inhibitor of IKKbeta-mediated activation of nuclear factor kappaB
    • Benfield CT, Mansur DS, McCoy LE, Ferguson BJ, Bahar MW, et al. (2011) Mapping the IkappaB kinase beta (IKKbeta)-binding interface of the B14 protein, a vaccinia virus inhibitor of IKKbeta-mediated activation of nuclear factor kappaB. J Biol Chem 286: 20727-20735.
    • (2011) J Biol Chem , vol.286 , pp. 20727-20735
    • Benfield, C.T.1    Mansur, D.S.2    McCoy, L.E.3    Ferguson, B.J.4    Bahar, M.W.5
  • 12
    • 77949443152 scopus 로고    scopus 로고
    • A poxvirus Bcl-2-like gene family involved in regulation of host immune response: sequence similarity and evolutionary history
    • Gonzalez JM, Esteban M, (2010) A poxvirus Bcl-2-like gene family involved in regulation of host immune response: sequence similarity and evolutionary history. Virol J 7: 59.
    • (2010) Virol J , vol.7 , pp. 59
    • Gonzalez, J.M.1    Esteban, M.2
  • 13
    • 4344600796 scopus 로고    scopus 로고
    • Poxvirus protein N1L targets the I-kappaB kinase complex, inhibits signaling to NF-kappaB by the tumor necrosis factor superfamily of receptors, and inhibits NF-kappaB and IRF3 signaling by toll-like receptors
    • DiPerna G, Stack J, Bowie AG, Boyd A, Kotwal G, et al. (2004) Poxvirus protein N1L targets the I-kappaB kinase complex, inhibits signaling to NF-kappaB by the tumor necrosis factor superfamily of receptors, and inhibits NF-kappaB and IRF3 signaling by toll-like receptors. J Biol Chem 279: 36570-36578.
    • (2004) J Biol Chem , vol.279 , pp. 36570-36578
    • DiPerna, G.1    Stack, J.2    Bowie, A.G.3    Boyd, A.4    Kotwal, G.5
  • 14
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden MS, Ghosh S, (2008) Shared principles in NF-kappaB signaling. Cell 132: 344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 15
    • 33750435582 scopus 로고    scopus 로고
    • NF-kappaB and the immune response
    • Hayden MS, West AP, Ghosh S, (2006) NF-kappaB and the immune response. Oncogene 25: 6758-6780.
    • (2006) Oncogene , vol.25 , pp. 6758-6780
    • Hayden, M.S.1    West, A.P.2    Ghosh, S.3
  • 16
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S, Uematsu S, Takeuchi O, (2006) Pathogen recognition and innate immunity. Cell 124: 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 17
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: outer membrane permeabilization and beyond
    • Tait SW, Green DR, (2010) Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 11: 621-632.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 18
    • 77958184901 scopus 로고    scopus 로고
    • Manipulation of host cell death pathways during microbial infections
    • Lamkanfi M, Dixit VM, (2010) Manipulation of host cell death pathways during microbial infections. Cell Host Microbe 8: 44-54.
    • (2010) Cell Host Microbe , vol.8 , pp. 44-54
    • Lamkanfi, M.1    Dixit, V.M.2
  • 21
    • 0031054439 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus encodes a functional bcl-2 homologue
    • Sarid R, Sato T, Bohenzky RA, Russo JJ, Chang Y, (1997) Kaposi's sarcoma-associated herpesvirus encodes a functional bcl-2 homologue. Nat Med 3: 293-298.
    • (1997) Nat Med , vol.3 , pp. 293-298
    • Sarid, R.1    Sato, T.2    Bohenzky, R.A.3    Russo, J.J.4    Chang, Y.5
  • 22
    • 0041885229 scopus 로고    scopus 로고
    • Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2
    • Huang Q, Petros AM, Virgin HW, Fesik SW, Olejniczak ET, (2003) Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2. J Mol Biol 332: 1123-1130.
    • (2003) J Mol Biol , vol.332 , pp. 1123-1130
    • Huang, Q.1    Petros, A.M.2    Virgin, H.W.3    Fesik, S.W.4    Olejniczak, E.T.5
  • 23
    • 0027260656 scopus 로고
    • Epstein-Barr virus-coded BHRF1 protein, a viral homologue of Bcl-2, protects human B cells from programmed cell death
    • Henderson S, Huen D, Rowe M, Dawson C, Johnson G, et al. (1993) Epstein-Barr virus-coded BHRF1 protein, a viral homologue of Bcl-2, protects human B cells from programmed cell death. Proc Natl Acad Sci USA 90: 8479-8483.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8479-8483
    • Henderson, S.1    Huen, D.2    Rowe, M.3    Dawson, C.4    Johnson, G.5
  • 25
    • 33745756937 scopus 로고    scopus 로고
    • A surface groove essential for viral Bcl-2 function during chronic infection in vivo
    • Loh J, Huang Q, Petros AM, Nettesheim D, van Dyk LF, et al. (2005) A surface groove essential for viral Bcl-2 function during chronic infection in vivo. PLoS Pathog 1: e10.
    • (2005) PLoS Pathog , vol.1
    • Loh, J.1    Huang, Q.2    Petros, A.M.3    Nettesheim, D.4    van Dyk, L.F.5
  • 26
    • 0030738667 scopus 로고    scopus 로고
    • Complete sequence and genomic analysis of murine gammaherpesvirus 68
    • Virgin HWt, Latreille P, Wamsley P, Hallsworth K, Weck KE, et al. (1997) Complete sequence and genomic analysis of murine gammaherpesvirus 68. J Virol 71: 5894-5904.
    • (1997) J Virol , vol.71 , pp. 5894-5904
    • Virgin, H.W.T.1    Latreille, P.2    Wamsley, P.3    Hallsworth, K.4    Weck, K.E.5
  • 27
    • 0037689535 scopus 로고    scopus 로고
    • Poxvirus immunomodulatory strategies: current perspectives
    • Johnston JB, McFadden G, (2003) Poxvirus immunomodulatory strategies: current perspectives. J Virol 77: 6093-6100.
    • (2003) J Virol , vol.77 , pp. 6093-6100
    • Johnston, J.B.1    McFadden, G.2
  • 28
    • 33947304650 scopus 로고    scopus 로고
    • A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak
    • Kvansakul M, van Delft MF, Lee EF, Gulbis JM, Fairlie WD, et al. (2007) A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak. Mol Cell 25: 933-942.
    • (2007) Mol Cell , vol.25 , pp. 933-942
    • Kvansakul, M.1    van Delft, M.F.2    Lee, E.F.3    Gulbis, J.M.4    Fairlie, W.D.5
  • 29
    • 33947727119 scopus 로고    scopus 로고
    • Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2
    • Douglas AE, Corbett KD, Berger JM, McFadden G, Handel TM, (2007) Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2. Protein Sci 16: 695-703.
    • (2007) Protein Sci , vol.16 , pp. 695-703
    • Douglas, A.E.1    Corbett, K.D.2    Berger, J.M.3    McFadden, G.4    Handel, T.M.5
  • 30
    • 0026787799 scopus 로고
    • Myxoma virus M11L ORF encodes a protein for which cell surface localization is critical in manifestation of viral virulence
    • Graham KA, Opgenorth A, Upton C, McFadden G, (1992) Myxoma virus M11L ORF encodes a protein for which cell surface localization is critical in manifestation of viral virulence. Virology 191: 112-124.
    • (1992) Virology , vol.191 , pp. 112-124
    • Graham, K.A.1    Opgenorth, A.2    Upton, C.3    McFadden, G.4
  • 31
    • 77951180715 scopus 로고    scopus 로고
    • Vaccinia virus F1L interacts with Bak using highly divergent Bcl-2 homology domains and replaces the function of Mcl-1
    • Campbell S, Hazes B, Kvansakul M, Colman P, Barry M, (2010) Vaccinia virus F1L interacts with Bak using highly divergent Bcl-2 homology domains and replaces the function of Mcl-1. J Biol Chem 285: 4695-4708.
    • (2010) J Biol Chem , vol.285 , pp. 4695-4708
    • Campbell, S.1    Hazes, B.2    Kvansakul, M.3    Colman, P.4    Barry, M.5
  • 32
    • 33745961009 scopus 로고    scopus 로고
    • Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis
    • Postigo A, Cross JR, Downward J, Way M, (2006) Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis. Cell Death Differ 13: 1651-1662.
    • (2006) Cell Death Differ , vol.13 , pp. 1651-1662
    • Postigo, A.1    Cross, J.R.2    Downward, J.3    Way, M.4
  • 33
    • 27644535708 scopus 로고    scopus 로고
    • The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation
    • Wasilenko ST, Banadyga L, Bond D, Barry M, (2005) The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation. J Virol 79: 14031-14043.
    • (2005) J Virol , vol.79 , pp. 14031-14043
    • Wasilenko, S.T.1    Banadyga, L.2    Bond, D.3    Barry, M.4
  • 34
    • 0344198504 scopus 로고    scopus 로고
    • Vaccinia virus encodes a previously uncharacterized mitochondrial-associated inhibitor of apoptosis
    • Wasilenko ST, Stewart TL, Meyers AF, Barry M, (2003) Vaccinia virus encodes a previously uncharacterized mitochondrial-associated inhibitor of apoptosis. Proc Natl Acad Sci USA 100: 14345-14350.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14345-14350
    • Wasilenko, S.T.1    Stewart, T.L.2    Meyers, A.F.3    Barry, M.4
  • 35
    • 52149113769 scopus 로고    scopus 로고
    • Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands
    • Kvansakul M, Yang H, Fairlie WD, Czabotar PE, Fischer SF, et al. (2008) Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands. Cell Death Differ 15: 1564-1571.
    • (2008) Cell Death Differ , vol.15 , pp. 1564-1571
    • Kvansakul, M.1    Yang, H.2    Fairlie, W.D.3    Czabotar, P.E.4    Fischer, S.F.5
  • 37
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle RJ, Strasser A, (2008) The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 9: 47-59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 38
    • 68149154728 scopus 로고    scopus 로고
    • BH3-only proteins and their roles in programmed cell death
    • Giam M, Huang DC, Bouillet P, (2008) BH3-only proteins and their roles in programmed cell death. Oncogene 27 (Suppl 1): S128-136.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Giam, M.1    Huang, D.C.2    Bouillet, P.3
  • 39
    • 70350738244 scopus 로고    scopus 로고
    • Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7
    • Oda S, Schroder M, Khan AR, (2009) Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7. Structure 17: 1528-1537.
    • (2009) Structure , vol.17 , pp. 1528-1537
    • Oda, S.1    Schroder, M.2    Khan, A.R.3
  • 40
    • 0036091728 scopus 로고    scopus 로고
    • Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis
    • Marani M, Tenev T, Hancock D, Downward J, Lemoine NR, (2002) Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis. Mol Cell Biol 22: 3577-3589.
    • (2002) Mol Cell Biol , vol.22 , pp. 3577-3589
    • Marani, M.1    Tenev, T.2    Hancock, D.3    Downward, J.4    Lemoine, N.R.5
  • 41
    • 33846964621 scopus 로고    scopus 로고
    • Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak
    • Willis SN, Fletcher JI, Kaufmann T, van Delft MF, Chen L, et al. (2007) Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science 315: 856-859.
    • (2007) Science , vol.315 , pp. 856-859
    • Willis, S.N.1    Fletcher, J.I.2    Kaufmann, T.3    van Delft, M.F.4    Chen, L.5
  • 42
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: how BH3-only proteins induce apoptosis
    • Willis SN, Adams JM, (2005) Life in the balance: how BH3-only proteins induce apoptosis. Curr Opin Cell Biol 17: 617-625.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 43
    • 57149135309 scopus 로고    scopus 로고
    • Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax
    • Lovell JF, Billen LP, Bindner S, Shamas-Din A, Fradin C, et al. (2008) Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. Cell 135: 1074-1084.
    • (2008) Cell , vol.135 , pp. 1074-1084
    • Lovell, J.F.1    Billen, L.P.2    Bindner, S.3    Shamas-Din, A.4    Fradin, C.5
  • 44
    • 34247497716 scopus 로고    scopus 로고
    • Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes
    • Leber B, Lin J, Andrews DW, (2007) Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes. Apoptosis 12: 897-911.
    • (2007) Apoptosis , vol.12 , pp. 897-911
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 45
    • 2942637332 scopus 로고    scopus 로고
    • Myxoma virus M11L prevents apoptosis through constitutive interaction with Bak
    • Wang G, Barrett JW, Nazarian SH, Everett H, Gao X, et al. (2004) Myxoma virus M11L prevents apoptosis through constitutive interaction with Bak. J Virol 78: 7097-7111.
    • (2004) J Virol , vol.78 , pp. 7097-7111
    • Wang, G.1    Barrett, J.W.2    Nazarian, S.H.3    Everett, H.4    Gao, X.5
  • 46
    • 54549114986 scopus 로고    scopus 로고
    • BAX activation is initiated at a novel interaction site
    • Gavathiotis E, Suzuki M, Davis ML, Pitter K, Bird GH, et al. (2008) BAX activation is initiated at a novel interaction site. Nature 455: 1076-1081.
    • (2008) Nature , vol.455 , pp. 1076-1081
    • Gavathiotis, E.1    Suzuki, M.2    Davis, M.L.3    Pitter, K.4    Bird, G.H.5
  • 47
    • 54149118187 scopus 로고    scopus 로고
    • Robust intrapulmonary CD8 T cell responses and protection with an attenuated N1L deleted vaccinia virus
    • Mathew A, O'Bryan J, Marshall W, Kotwal GJ, Terajima M, et al. (2008) Robust intrapulmonary CD8 T cell responses and protection with an attenuated N1L deleted vaccinia virus. PLoS One 3: e3323.
    • (2008) PLoS One , vol.3
    • Mathew, A.1    O'Bryan, J.2    Marshall, W.3    Kotwal, G.J.4    Terajima, M.5
  • 48
    • 79952590431 scopus 로고    scopus 로고
    • N1L is an ectromelia virus virulence factor and essential for in vivo spread upon respiratory infection
    • Gratz MS, Suezer Y, Kremer M, Volz A, Majzoub M, et al. (2011) N1L is an ectromelia virus virulence factor and essential for in vivo spread upon respiratory infection. J Virol 85: 3557-3569.
    • (2011) J Virol , vol.85 , pp. 3557-3569
    • Gratz, M.S.1    Suezer, Y.2    Kremer, M.3    Volz, A.4    Majzoub, M.5
  • 49
    • 37048999786 scopus 로고    scopus 로고
    • A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes
    • Gloeckner CJ, Boldt K, Schumacher A, Roepman R, Ueffing M, (2007) A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes. Proteomics 7: 4228-4234.
    • (2007) Proteomics , vol.7 , pp. 4228-4234
    • Gloeckner, C.J.1    Boldt, K.2    Schumacher, A.3    Roepman, R.4    Ueffing, M.5
  • 50
    • 34547408207 scopus 로고    scopus 로고
    • Retroviral transduction of DT40
    • Randow F, Sale JE, (2006) Retroviral transduction of DT40. Subcell Biochem 40: 383-386.
    • (2006) Subcell Biochem , vol.40 , pp. 383-386
    • Randow, F.1    Sale, J.E.2
  • 51
    • 33744818439 scopus 로고    scopus 로고
    • Vaccinia virus strain Western Reserve protein B14 is an intracellular virulence factor
    • Chen RA, Jacobs N, Smith GL, (2006) Vaccinia virus strain Western Reserve protein B14 is an intracellular virulence factor. J Gen Virol 87: 1451-1458.
    • (2006) J Gen Virol , vol.87 , pp. 1451-1458
    • Chen, R.A.1    Jacobs, N.2    Smith, G.L.3
  • 52
    • 0027980628 scopus 로고
    • Vaccinia virus gene A36R encodes a M(r) 43-50 K protein on the surface of extracellular enveloped virus
    • Parkinson JE, Smith GL, (1994) Vaccinia virus gene A36R encodes a M(r) 43-50 K protein on the surface of extracellular enveloped virus. Virology 204: 376-390.
    • (1994) Virology , vol.204 , pp. 376-390
    • Parkinson, J.E.1    Smith, G.L.2
  • 54
    • 58849123669 scopus 로고    scopus 로고
    • Refinement with Local Structure Similarity Restraints (LSSR) Enables Exploitation of Information from Related Structures and Facilitates use of NCS
    • Smart OS, Brandl M, Flensburg C, Keller P, Paciorek W, et al. (2008) Refinement with Local Structure Similarity Restraints (LSSR) Enables Exploitation of Information from Related Structures and Facilitates use of NCS. Abstr Annu Meet Am Crystallogr Assoc Abstract TP139: 117.
    • (2008) Abstr Annu Meet Am Crystallogr Assoc Abstract , vol.TP139 , pp. 117
    • Smart, O.S.1    Brandl, M.2    Flensburg, C.3    Keller, P.4    Paciorek, W.5
  • 56
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 57
    • 0025302978 scopus 로고
    • Transient dominant selection of recombinant vaccinia viruses
    • Falkner FG, Moss B, (1990) Transient dominant selection of recombinant vaccinia viruses. J Virol 64: 3108-3111.
    • (1990) J Virol , vol.64 , pp. 3108-3111
    • Falkner, F.G.1    Moss, B.2
  • 58
    • 0023935968 scopus 로고
    • A dominant selectable marker for the construction of recombinant poxviruses
    • Boyle DB, Coupar BE, (1988) A dominant selectable marker for the construction of recombinant poxviruses. Gene 65: 123-128.
    • (1988) Gene , vol.65 , pp. 123-128
    • Boyle, D.B.1    Coupar, B.E.2
  • 59
    • 0026017350 scopus 로고
    • Vaccinia virus DNA ligase is nonessential for virus replication: recovery of plasmids from virus-infected cells
    • Kerr SM, Smith GL, (1991) Vaccinia virus DNA ligase is nonessential for virus replication: recovery of plasmids from virus-infected cells. Virology 180: 625-632.
    • (1991) Virology , vol.180 , pp. 625-632
    • Kerr, S.M.1    Smith, G.L.2
  • 60
    • 0019778338 scopus 로고
    • Identification of DNA sequences required for transcription of the human alpha 1-globin gene in a new SV40 host-vector system
    • Mellon P, Parker V, Gluzman Y, Maniatis T, (1981) Identification of DNA sequences required for transcription of the human alpha 1-globin gene in a new SV40 host-vector system. Cell 27: 279-288.
    • (1981) Cell , vol.27 , pp. 279-288
    • Mellon, P.1    Parker, V.2    Gluzman, Y.3    Maniatis, T.4
  • 61
    • 20144372620 scopus 로고    scopus 로고
    • High-throughput mapping of a dynamic signaling network in mammalian cells
    • Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, et al. (2005) High-throughput mapping of a dynamic signaling network in mammalian cells. Science 307: 1621-1625.
    • (2005) Science , vol.307 , pp. 1621-1625
    • Barrios-Rodiles, M.1    Brown, K.R.2    Ozdamar, B.3    Bose, R.4    Liu, Z.5
  • 62
    • 0026646637 scopus 로고
    • A soluble receptor for interleukin-1 beta encoded by vaccinia virus: a novel mechanism of virus modulation of the host response to infection
    • Alcami A, Smith GL, (1992) A soluble receptor for interleukin-1 beta encoded by vaccinia virus: a novel mechanism of virus modulation of the host response to infection. Cell 71: 153-167.
    • (1992) Cell , vol.71 , pp. 153-167
    • Alcami, A.1    Smith, G.L.2
  • 63
    • 0036327752 scopus 로고    scopus 로고
    • Dermal infection with vaccinia virus reveals roles for virus proteins not seen using other inoculation routes
    • Tscharke DC, Reading PC, Smith GL, (2002) Dermal infection with vaccinia virus reveals roles for virus proteins not seen using other inoculation routes. J Gen Virol 83: 1977-1986.
    • (2002) J Gen Virol , vol.83 , pp. 1977-1986
    • Tscharke, D.C.1    Reading, P.C.2    Smith, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.